Zobrazeno 1 - 10
of 30
pro vyhledávání: '"Hannu Pösö"'
Publikováno v:
Acta Pharmacologica et Toxicologica. 57:250-254
The activity of coumarin 7-hydroxylase (coumarin 7-hydroxylation) was inhibited in B6 mouse liver after a single injection of methylglyoxal bis(guanylhydrazone (MGBG). The decrease in the activity in vivo was greatest (70%) one day after the drug inj
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::41b628fe68eb9c7eef3315edcb6d5baf
https://doi.org/10.1111/j.1600-0773.1985.tb00039.x
https://doi.org/10.1111/j.1600-0773.1985.tb00039.x
Autor:
Hannu Pösö
Publikováno v:
Pharmacology Biochemistry and Behavior. 13:83-88
The effect of ethanol on the activity of ornithine decarboxylase (ODC), tyrosine aminotransferase (TAT), alanine aminotransferase (ALAT) and lactate dehydrogenase (LD), as well as on protein concentration, was studied in regenerating rat liver after
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::61acc977b8e8924eb48bb05d98230fbe
https://doi.org/10.1016/s0091-3057(80)80013-x
https://doi.org/10.1016/s0091-3057(80)80013-x
Autor:
Malla Kuosmanen, Hannu Pösö
Publikováno v:
FEBS Letters. 179:17-20
Physiological concentrations (0.5–2.0 mM) of spermidine and spermine were observed to inhibit the digestion in vitro of plasmid pJDB 207 by the restriction endonucleases Bam HI (EC 3.1.23.6), Eco RI (EC 3.2.23.13), Hin dIII (EC 3.1.23.20), Hpa I (E
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1ace96086f9243ea474ebbdd3d719932
https://doi.org/10.1016/0014-5793(85)80181-2
https://doi.org/10.1016/0014-5793(85)80181-2
Publikováno v:
FEMS Microbiology Letters. 19:299-302
We report here that C. thermohydrosulfuricum contains an unusual distribution of polyamines and a characteristic propylamine transferase activity that can use 1,3-diaminopropane as the substrate in the synthesis of thermine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bc831019dfbb642fea7eaba5c8cea973
https://doi.org/10.1111/j.1574-6968.1983.tb00561.x
https://doi.org/10.1111/j.1574-6968.1983.tb00561.x
Publikováno v:
Journal of Biological Chemistry. 259:12307-12310
A human neuroblastoma cell line (Paju) was resistant to 10 mM difluoromethylornithine, a concentration at which the growth of all mammalian cells normally stops. Ornithine decarboxylase from Paju was very resistant to inhibition by difluoromethylorni
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ca469cb16baf11200ca09b2c394ee169
https://doi.org/10.1016/s0021-9258(18)90742-8
https://doi.org/10.1016/s0021-9258(18)90742-8
Publikováno v:
Biochemical and Biophysical Research Communications. 114:779-784
Several Acetobacteria contained large amounts of spermine in addition to the putrescine and spermidine, which are the polyamines normally found in prokaryotes. A spermine synthase present in cell extracts of these Acetobacteria is the first example o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fe748aa366893a70f4e4ea86ef6a2c9c
https://doi.org/10.1016/0006-291x(83)90849-5
https://doi.org/10.1016/0006-291x(83)90849-5
Publikováno v:
European Journal of Immunology. 15:783-787
The T cell mitogens, concanavalin A and the monoclonal antibody OKT3, cause a rapid activation of ornithine decarboxylase (ODC) activity in human T lymphocytes, maximal within 10 min of mitogen addition. Nonmitogenic ligands to T cell surface structu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2466aff55325479dd8390537065fa9b2
https://doi.org/10.1002/eji.1830150808
https://doi.org/10.1002/eji.1830150808
Autor:
Hannu Pösö, Eija Karvonen
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 791:239-243
The activities of ornithine decarboxylase and spermidine N1-acetyltransferase started to rise in normal rat liver 4 h after the intraperitoneal injection of methylglyoxal bis(guanylhydrazone) (MGBG; 80 mg/kg). Ornithine decarboxylase had its greatest
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8700bb2986b27540d77c17ef6b575ece
https://doi.org/10.1016/0167-4838(84)90014-1
https://doi.org/10.1016/0167-4838(84)90014-1
Publikováno v:
Biochemical and Biophysical Research Communications. 126:96-102
A human neuroblastoma cell line (Paju) grew in 10 mM difluoromethyl-ornithine, which at this concentration normally stops the growth of all mammalian cells. Ornithine decarboxylase from Paju was resistant to inhibition in vitro by difluoromethylornit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::08a8235e49db063fb272a4dbce30b340
https://doi.org/10.1016/0006-291x(85)90576-5
https://doi.org/10.1016/0006-291x(85)90576-5
Publikováno v:
Journal of Biological Chemistry. 257:7549-7553
Treatment of male mice with excess androgens increased the activity of renal ornithine decarboxylase 60-fold in the BALB/c strain and 4-fold in the CD-1 strain. Part of the increase in the activity of ornithine decarboxylase was due to a decreased ra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5184c6a8b992a6b3ee9e9cb07d543956
https://doi.org/10.1016/s0021-9258(18)34414-4
https://doi.org/10.1016/s0021-9258(18)34414-4